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J Biol Chem, Vol. 273, Issue 33, 20860-20866, August 14, 1998
From the Department of Chemistry, Faculty of Science, Kyushu
University, Fukuoka 812-8581, Japan
Cytochrome b5 (b5), a
typical tail-anchored protein of the endoplasmic reticulum (ER)
membrane, is composed of three functionally different domains:
amino-terminal heme-containing catalytic, central hydrophobic
membrane-anchoring, and carboxyl-terminal ER-targeting domains (Mitoma,
J., and Ito, A. (1992) EMBO J. 11, 4197-4203). To analyze
the potential retention signal of b5, mutant proteins were prepared to
replace each domain with natural or artificial sequences, and
subcellular localizations were examined using immunofluorescence microscopy and cell fractionation. The transmembrane domain functioned to retain the cytochrome in the ER, and the mutation of all or part of
the transmembrane domain with an artificial hydrophobic sequence had
practically no effect on intracellular distribution of the cytochrome.
However, when the transmembrane domain was extended systematically, a
substantial portion of the protein with the domain of over 22 amino
acid residues leaked from the organelle. Thus, the transmembrane length
functions as the retention signal. When cytochromes with mutations at
the carboxyl-terminal end were overexpressed in cells, a substantial
portion of the protein was transported to the plasma membrane,
indicating that the carboxyl-terminal luminal domain also has a role in
retention of b5 in the ER. Carbohydrate moiety of the
glycosylatably-mutated b5 was sensitive to endoglycosidase H but
resistant to endoglycosidase D. Therefore, both transmembrane and
carboxyl-terminal portions seems to function as the static retention
signal.
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